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P81065

- GST_OCHAN

UniProt

P81065 - GST_OCHAN

Protein

Glutathione S-transferase

Gene

gst

Organism
Ochrobactrum anthropi
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 66 (01 Oct 2014)
      Sequence version 2 (30 May 2000)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.1 Publication

    Kineticsi

    1. KM=0.132 mM for glutathione1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei10 – 101Glutathione1 Publication
    Binding sitei35 – 351Glutathione1 Publication
    Binding sitei52 – 521Glutathione; via amide nitrogen and carbonyl oxygen1 Publication
    Binding sitei105 – 1051Glutathione1 Publication

    GO - Molecular functioni

    1. glutathione transferase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Transferase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase (EC:2.5.1.18)
    Gene namesi
    Name:gst
    OrganismiOchrobactrum anthropi
    Taxonomic identifieri529 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeOchrobactrum

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi10 – 101C → A: Strongly reduced affinity for glutathione. Reduces enzyme activity by about 50%. 2 Publications
    Mutagenesisi11 – 111S → A: Reduced activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 201201Glutathione S-transferasePRO_0000185973Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.By similarity

    Structurei

    Secondary structure

    1
    201
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi2 – 54
    Helixi12 – 2110
    Beta strandi26 – 294
    Turni32 – 354
    Helixi43 – 453
    Beta strandi54 – 585
    Beta strandi61 – 655
    Helixi66 – 7510
    Helixi80 – 823
    Helixi89 – 10921
    Helixi110 – 1123
    Helixi118 – 13821
    Beta strandi148 – 1503
    Helixi153 – 16715
    Helixi176 – 18611
    Helixi189 – 1979

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2NTOX-ray2.10A1-201[»]
    2PVQX-ray1.80A1-201[»]
    ProteinModelPortaliP81065.
    SMRiP81065. Positions 1-201.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP81065.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1 – 8181GST N-terminalAdd
    BLAST
    Domaini87 – 201115GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni65 – 662Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Beta family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF13409. GST_N_2. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P81065-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLYYKVGAC SLAPHIILSE AGLPYELEAV DLKAKKTADG GDYFAVNPRG    50
    AVPALEVKPG TVITQNAAIL QYIGDHSDVA AFKPAYGSIE RARLQEALGF 100
    CSDLHAAFSG LFAPNLSEEA RAGVIANINR RLGQLEAMLS DKNAYWLGDD 150
    FTQPDAYASV IIGWGVGQKL DLSAYPKALK LRERVLARPN VQKAFKEEGL 200
    N 201
    Length:201
    Mass (Da):21,739
    Last modified:May 30, 2000 - v2
    Checksum:i763B2D3DECA21F2D
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y17279 Genomic DNA. Translation: CAA76728.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    Y17279 Genomic DNA. Translation: CAA76728.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2NTO X-ray 2.10 A 1-201 [» ]
    2PVQ X-ray 1.80 A 1-201 [» ]
    ProteinModelPortali P81065.
    SMRi P81065. Positions 1-201.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P81065.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF13409. GST_N_2. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning, expression and site-directed mutagenesis of glutathione S-transferase from Ochrobactrum anthropi."
      Favaloro B., Tamburro A., Angelucci S., de Luca A., di Ilio C., Rotilio D.
      Biochem. J. 335:573-579(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-25 AND 50-74, MUTAGENESIS.
    2. "Purification and characterization of a novel glutathione transferase from Ochrobactrum anthropi."
      Favaloro B., Melino S., Petruzzelli R., di Ilio C., Rotilio D.
      FEMS Microbiol. Lett. 160:81-86(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 1-25.
    3. "Cysteine 10 is critical for the activity of Ochrobactrum anthropi glutathione transferase and its mutation to alanine causes the preferential binding of glutathione to the H-site."
      Allocati N., Federici L., Masulli M., Favaloro B., Di Ilio C.
      Proteins 71:16-23(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH GLUTATHIONE, CATALYTIC ACTIVITY, MUTAGENESIS OF CYS-10, BIOPHYSICOCHEMICAL PROPERTIES.

    Entry informationi

    Entry nameiGST_OCHAN
    AccessioniPrimary (citable) accession number: P81065
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1998
    Last sequence update: May 30, 2000
    Last modified: October 1, 2014
    This is version 66 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3